2VUQ
Crystal structure of a human tRNAGly acceptor stem microhelix (derived from the gene sequence DG9990) at 1.18 Angstroem resolution
Summary for 2VUQ
Entry DOI | 10.2210/pdb2vuq/pdb |
Descriptor | 5'-R(*GP*CP*AP*UP*UP*GP*GP)-3', 5'-R(*CP*CP*AP*AP*UP*GP*CP)-3' (3 entities in total) |
Functional Keywords | class ii aminoacyl-trna / synthetase system, rna, trna identity elements, glycyl-trna-synthetase (glyrs), isoacceptors, human trnagly, aminoacyl-trna-stem |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 2 |
Total formula weight | 4417.75 |
Authors | Eichert, A.,Perbandt, M.,Schreiber, A.,Fuerste, J.P.,Betzel, C.,Erdmann, V.A.,Foerster, C. (deposition date: 2008-05-29, release date: 2009-03-10, Last modification date: 2023-12-13) |
Primary citation | Eichert, A.,Perbandt, M.,Schreiber, A.,Fuerste, J.P.,Betzel, C.,Erdmann, V.A.,Foerster, C. Crystal Structure of the Human Trnagly Microhelix Isoacceptor G9990 at 1.18 A Resolution Biochem.Biophys.Res.Commun., 380:503-, 2009 Cited by PubMed Abstract: The tRNA(Gly)/Glycyl-tRNA synthetase system belongs to the so called 'class II' in which tRNA identity elements consist of relative few and simple motifs, as compared to 'class I' where the tRNA determinants are more complicated and spread over different parts of the tRNA, mostly including the anticodon. The determinants from 'class II' although, are located in the aminoacyl stem and sometimes include the discriminator base. There exist predominant structure differences for the Glycyl-tRNA-synthetases and for the tRNA(Gly) identity elements comparing eucaryotic/archaebacterial and eubacterial systems. We focus on comparative X-ray structure analysis of tRNA(Gly) acceptor stem microhelices from different organisms. Here, we report the X-ray structure of the human tRNA(Gly) microhelix isoacceptor G9990 at 1.18A resolution. Superposition experiments to another human tRNA(Gly) microhelix and a detailed comparison of the RNA hydration patterns show a great number of water molecules with identical positions in both RNAs. This is the first structure comparison of hydration layers from two isoacceptor tRNA microhelices with a naturally occurring base pair exchange. PubMed: 19284994DOI: 10.1016/J.BBRC.2009.01.127 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.18 Å) |
Structure validation
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